Separation of Monoclonal Antibody Monomer from its High and Low Molar Mass Impurities Using Size Exclusion and Reversed Phase Chromatography
Event Date: October 01, 2013 at 02:00 PM EDT

Due to their use in the field of biotherapeutics, the analysis of monoclonal antibodies is becoming increasingly popular. Biotherapeutic proteins must be free from aggregates, because protein aggregates are high molar mass species that are often toxic and implicated in a wide variety of diseases. Thus, the pure monoclonal antibody monomer must be well resolved from its dimer and higher order aggregates.

Size exclusion chromatography (SEC) is effective in separating and quantitating the aggregates or high molar mass species as a function of their hydrodynamic volume, while reversed phase chromatography (RPC) is useful for the separation of large biomolecules, such as proteins and their hydrophobic variants.

This webcast will discuss the use of these two different modes of chromatography (SEC and RPC) for the analysis of monoclonal antibodies, specifically the separation of a monomer from its high and low molar mass impurities and variants.

• Protein aggregates are high molar mass species that are often toxic and implicated in a wide variety of diseases.
• Monoclonal antibodies (mAb) are being investigated as biotherapeutic drugs for the treatment of several diseases.
• HPLC methods developed using analytical SEC and RPC columns ensure the removal and quantitation of high molar mass aggregates and low molar mass fragments.


Moderator:

Steve Brown

Technical Editor
LCGC

Speaker:

Justin Steve

Technical Services Specialist
Tosoh Bioscience


IMPORTANT - PLEASE READ
This is a FREE streaming audio Webcast and does not require a phone line. If you have any questions regarding this Webcast, please contact Kristen Farrell, kfarrell@advanstar.com.

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If you are currently analyzing monoclonal antibodies, which column are you using for your analysis? (can choose more than one)*TSKgel SEC columns
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